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  • Title: Phosphorylation by cyclic AMP-dependent protein kinase does not affect the association of ATP citrate-lyase with isolated mitochondria.
    Author: Lin TW, Bridger WA.
    Journal: FEBS Lett; 1987 Nov 30; 224(2):322-4. PubMed ID: 2826229.
    Abstract:
    ATP citrate-lyase is known to be a substrate for various protein kinases, but the functional role, if any, of kinase-directed phosphorylation of this enzyme has not been identified. Recently, Strålfors [(1987) J. Biol. Chem. 262, 11486-11489] has suggested that effects on the association of this enzyme with mitochondria may account for the observed ability of isoproteronol or insulin to promote immobilization of ATP citrate-lyase in permeabilized cells. Here we report studies involving phosphorylation of the pure enzyme in vitro using cyclic AMP-dependent protein kinase. We show that phosphorylation has no significant effect on the fraction of the enzyme that may be bound to isolated mitochondria.
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